dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: FGRAMPH1_01T19927-p1

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Basic Information help

Species

Fusarium graminearum

Lineage

Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium graminearum

CAZyme ID

FGRAMPH1_01T19927-p1

CAZy Family

GH47

CAZyme Description

glucoamylase precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
667		71543.72	4.9016

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FgraminearumPH-1	14145	229533	2	14143

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.3:94	1.14.99.55:4

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH15	81	492	3.7e-78	0.9833795013850416
CBM20	566	656	2.1e-29	0.9666666666666667

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	2.63e-139	75	492	2	416	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886	CBM20_glucoamylase	3.31e-56	560	665	1	106	Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557	CBM_20	7.03e-38	566	657	1	91	Starch binding domain.
99883	CBM20_alpha_amylase	7.18e-31	566	665	1	94	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
215006	CBM_2	5.35e-30	566	653	1	88	Starch binding domain.

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
1	667	1	667
1	667	1	667
10	667	1	658
10	667	1	654
35	667	1	629

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.25e-284	64	667	1	599	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.83e-224	63	666	1	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.51e-207	64	666	7	593	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6.16e-193	63	532	1	467	Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
3.52e-192	63	532	1	466	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.59e-259	35	666	1	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
7.57e-224	61	666	23	640	Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
7.57e-224	61	666	23	640	Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
1.04e-223	54	666	16	639	Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
2.73e-221	61	666	23	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000036	0.000007

TMHMM Annotations help

There is no transmembrane helices in FGRAMPH1_01T19927-p1.